Format

Send to

Choose Destination
Mol Neurodegener. 2015 Dec 8;10:66. doi: 10.1186/s13024-015-0062-3.

α-synuclein interacts with SOD1 and promotes its oligomerization.

Author information

1
Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany.
2
Mayo Clinic, Jacksonville, Florida, USA.
3
Department of Neurology, Ulm University, Albert-Einstein-Allee 11, 89081, Ulm, Germany. karin.danzer@uni-ulm.de.

Abstract

BACKGROUND:

Parkinson's disease (PD) and amyotrophic lateral sclerosis (ALS) are both neurodegenerative diseases leading to impaired execution of movement. α-Synuclein plays a central role in the pathogenesis of PD whereas Cu, Zn superoxide dismutase (SOD1) is a key player in a subset of familial ALS cases. Under pathological conditions both α-synuclein and SOD1 form oligomers and fibrils. In this study we investigated the possible molecular interaction of α-synuclein and SOD1 and its functional and pathological relevance.

RESULTS:

Using a protein-fragment complementation approach and co-IP, we found that α-synuclein and SOD1 physically interact in living cells, human erythrocytes and mouse brain tissue. Additionally, our data show that disease related mutations in α-synuclein (A30P, A53T) and SOD1 (G85R, G93A) modify the binding of α-synuclein to SOD1. Notably, α-synuclein accelerates SOD1 oligomerization independent of SOD1 activity.

CONCLUSION:

This study provides evidence for a novel interaction of α-synuclein and SOD1 that might be relevant for neurodegenerative diseases.

PMID:
26643113
PMCID:
PMC4672499
DOI:
10.1186/s13024-015-0062-3
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for BioMed Central Icon for PubMed Central
Loading ...
Support Center